Imaging the Glycome in Living Systems

Li, Boyangzi; Mock, Feiyan; Wu, Peng

doi:10.1016/b978-0-12-388448-0.00029-2

Cited by 9 publications

(9 citation statements)

References 64 publications

(92 reference statements)

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“…Although much effort has been spent on glycobiomarkers research, clinicians and medicinal chemists rarely consider glycans as biological targets or drugs [ 224 ], hindering advances in bladder cancer management and in the development of targeted therapeutics. Notwithstanding, this unfamiliarity is beginning to change as improved methods for carbohydrate synthesis [ 225 - 227 ], sequencing [ 228 , 229 ], and biological analysis [ 230 - 232 ] become more sensitive and widely available.…”

Section: Prognosis Glycomarkers For Bladder Cancermentioning

confidence: 99%

Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?

et al. 2017

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The high molecular heterogeneity of bladder tumours is responsible for significant variations in disease course, as well as elevated recurrence and progression rates, thereby hampering the introduction of more effective targeted therapeutics. The implementation of precision oncology settings supported by robust molecular models for individualization of patient management is warranted. This effort requires a comprehensive integration of large sets of panomics data that is yet to be fully achieved. Contributing to this goal, over 40 years of bladder cancer glycobiology have disclosed a plethora of cancer-specific glycans and glycoconjugates (glycoproteins, glycolipids, proteoglycans) accompanying disease progressions and dissemination. This review comprehensively addresses the main structural findings in the field and consequent biological and clinical implications. Given the cell surface and secreted nature of these molecules, we further discuss their potential for non-invasive detection and therapeutic development. Moreover, we highlight novel mass-spectrometry-based high-throughput analytical and bioinformatics tools to interrogate the glycome in the postgenomic era. Ultimately, we outline a roadmap to guide future developments in glycomics envisaging clinical implementation.

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Section: Prognosis Glycomarkers For Bladder Cancermentioning

confidence: 99%

Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?

et al. 2017

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“…Imaging techniques are typically employed for spatial and temporal analysis of molecules in cells and tissues and are widely employed for protein and, more recently, glycan analysis. 400,401 However, image analysis of specific protein glycoforms remains a significant challenge. Several laboratories have combined oligosaccharide metabolic labeling with protein labeling to image protein glycoforms using FRET-based microscopies.…”

Section: Summary and Future Outlookmentioning

confidence: 99%

“…Although MS is capable of identifying thousands of proteins in a given sample with high accuracy and reproducibility, their spatiotemporal relationships are typically lost in such experiments. Imaging techniques are typically employed for spatial and temporal analysis of molecules in cells and tissues and are widely employed for protein and, more recently, glycan analysis. , However, image analysis of specific protein glycoforms remains a significant challenge. Several laboratories have combined oligosaccharide metabolic labeling with protein labeling to image protein glycoforms using FRET-based microscopies. − In addition, protein-specific aptamers have been used to direct selective labeling to nearby glycans .…”

Section: Summary and Future Outlookmentioning

confidence: 99%

Chemical Glycoproteomics

Palaniappan

Bertozzi²

2016

Chem. Rev.

234

205

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Chemical tools have accelerated progress in glycoscience, reducing experimental barriers to studying protein glycosylation, the most widespread and complex form of posttranslational modification. For example, chemical glycoproteomics technologies have enabled the identification of specific glycosylation sites and glycan structures that modulate protein function in a number of biological processes. This field is now entering a stage of logarithmic growth, during which chemical innovations combined with mass spectrometry advances could make it possible to fully characterize the human glycoproteome. In this review, we describe the important role that chemical glycoproteomics methods are playing in such efforts. We summarize developments in four key areas: enrichment of glycoproteins and glycopeptides from complex mixtures, emphasizing methods that exploit unique chemical properties of glycans or introduce unnatural functional groups through metabolic labeling and chemoenzymatic tagging; identification of sites of protein glycosylation; targeted glycoproteomics; and functional glycoproteomics, with a focus on probing interactions between glycoproteins and glycan-binding proteins. Our goal with this survey is to provide a foundation on which continued technological advancements can be made to promote further explorations of protein glycosylation.

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“…Azide groups can react with the complementary phosphines via the Staudinger ligation [15,16], linear alkynes via the Cu-catalyzed azide-alkyne cycloaddition (CuAAC) [16,17], and cyclooctynes via the strain-promoted azide-alkyne cycloaddition (SAAC), also termed "Cu-free click chemistry" [16][17][18][19][20]. MGE has been successfully applied for in situ imaging of glycans in different cell lines and living organisms [21][22][23][24][25][26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Bioorthogonal Labeling Reveals Different Expression of Glycans in Mouse Hippocampal Neuron Cultures during Their Development

et al. 2020

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The expression of different glycans at the cell surface dictates cell interactions with their environment and other cells, being crucial for the cell fate. The development of the central nervous system is associated with tremendous changes in the cell glycome that is tightly regulated. Herein, we have employed bioorthogonal Cu-free click chemistry to image temporal distribution of different glycans in live mouse hippocampal neurons during their maturation in vitro. We show development-dependent glycan patterns with increased fucose and decreased mannose expression at the end of the maturation process. We also demonstrate that this approach is biocompatible and does not affect glycan transport although it relies on an administration of modified glycans. The applicability of this strategy to tissue sections unlocks new opportunities to study the glycan dynamics under more complex physiological conditions.

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Imaging the Glycome in Living Systems

Cited by 9 publications

References 64 publications

Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?

Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?

Chemical Glycoproteomics

Bioorthogonal Labeling Reveals Different Expression of Glycans in Mouse Hippocampal Neuron Cultures during Their Development

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